Microbiology and Immunology
Columbus Center, 701 E. Pratt Street, Room 5041, Baltimore, MD 21202
Education and Training
University of Cape Town, General Physiology B.Sc. (Hons) (First Class) 1969
University of California, Riverside, (Biology). Ph.D. 1972.
University of California, San Diego, 1973.
Univ. of Chicago, Argonne National Laboratory, 1974.
2010- Professor, Inst. of Marine and Environmental Technology, U Maryland
2010- Professor, Dept. Microbiology and Immunology, U Maryland Med School
1995-2010 Professor, Center of Marine Biotechnology, U Maryland Biotech. Inst
1996-97 Director, and Associate Director (2001-07), Center of Marine Biotechnology
1989-95 Associate Professor, Center of Marine Biotechnology,
1982-88 Associate Professor, Dept. of Microbiology, Univ. of Cape Town
1982 Visiting Professor, Genetics Institute, Univ. of Bayreuth, West Germany
1985-86 Visiting Scientist, NIADDK, National Institutes of Health
1980-88 Senior Lecturer, Dept. of Microbiology, Univ. of Cape Town
1979-80 Visiting Scientist, Dept. of Genetics, Univ. of Washington, Seattle, WA
1974-79 Lecturer/Senior Lecturer, Dept. of Microbiology, Rhodes Univ., South Africa
Extremophiles; Model organisms; Protein folding; Chaperones, Chaperonopathy
Antranikian G, Suleiman M, Schäfers C, Adams MWW, Bartolucci S, Blamey JM, Birkeland NK, Bonch-Osmolovskaya E, da Costa MS, Cowan D, Danson M, Forterre P, Kelly R, Ishino Y, Littlechild J, Moracci M, Noll K, Oshima T, Robb FT, Rossi M, Santos H, Schönheit P, Sterner R, Thauer R, Thomm M, Wiegel J, Stetter KO (2017) Diversity of bacteria and archaea from two shallow marine hydrothermal vents from Vulcano Island.) Extremophiles. 21(4):733-742. doi: 10.1007/s00792-017-0938-y
Spigolon, D, D. T Gallagher, A Velazquez-Campoy, D Bulone, J Narang, P L San Biagio, F Cappello, A J.L. Macario, E Conway de Macario, FT Robb. (2017). Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog. Biochemistry and Biophysics Reports 12:66-71 . DOI: 10.1016/j.bbrep.2017.07.011 ·
Conway de Macario E, Robb FT, Macario AJ. (2017) Prokaryotic Chaperonins as Experimental Models for Elucidating Structure-Function Abnormalities of Human Pathogenic Mutant Counterparts. Front Mol Biosci. 9;3:84. doi: 10.3389/fmolb.2016.00084.
An, Y J*, Rowland, SE*, Na, JH*, Spigolon, D, Hong S K, Yoon Y J, Lee, JH, Cha, S S, FT Robb (2017). Structural and mechanistic characterization of a novel archaeal-like chaperonin from a thermophilic bacterium. Nature Communications, 8:827 DOI: 10.1038/s41467-017-00980-z. *Authors contributed equally
Rowland, SE and Robb FT (2017) "Structure, Function and Evolution of the Hsp60 Chaperonins" in Heat Shock Proteins, Vol. 11, Santosh C. M. Kumar and Shekhar C. Mande (Eds): Prokaryotic Chaperonins, 978-981-10-4650-6. Springer. http://www.springer.com/us/book/9789811046506.
Vetriani, C and FT Robb (2017). Scientia online article on University of Maryland/Rutgers University collaboration:
Brumm P, DA Mead, K Gowda and FT Robb (2016) The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM 6724™ reveals a specialized carbohydrate fermentor. Front. Microbiol. - Extreme Microbiology (in press).
An YJ, Rowland SE, Robb FT, Cha SS. (2016) Purification, crystallization, and preliminary X-ray crystallographic analysis of the Group III chaperonin from Carboxydothermus hydrogenoformans. J Microbiol.54(6):440-4. doi: 10.1007/s12275-016-6089-5.
Sant'Anna FH, Lebedinsky AV, Sokolova TG, Robb FT, Gonzalez JM. (2015) Analysis of three genomes within the thermophilic bacterial species Caldanaerobacter subterraneus with a focus on carbon monoxide dehydrogenase evolution and hydrolase diversity. BMC Genomics. 2015 Oct 7;16:757. doi: 10.1186/s12864-015-1955-9.
Min W, Angileri F, Luo H, Lauria A, Shanmugasundaram M, Almerico AM, Cappello F, de Macario EC, Lednev IK, Macario AJ, Robb FT. (2014) A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model. Sci Rep. 4:6688. doi: 10.1038/srep06688.
Kurouski D, Luo H, Sereda V, Robb FT, Lednev IK. (2013) Deconstruction of stable cross-beta fibrillar structures into toxic and nontoxic products using a mutated archaeal chaperonin. ACS Chem. Biol. 8(9):2095-101. doi: 10.1021/cb400238a. PMID:2387567
Techtmann SM, Colman AS, Lebedinsky AV, Sokolova TG and Robb FT (2012) Evidence for horizontal gene transfer of anaerobic carbon monoxide dehydrogenases. Frontiers in Evolutionary and Genomic Microbiology. 3: 132 doi: 10.3389/fmicb.2012.00132. PMID:22529840 | PMCID:PMC3328121
Kurouski,D, Luo, H, Sereda, V, Robb FT and Lednev IK. (2012) Rapid degradation kinetics of amyloid fibrils under mild conditions by an archaeal chaperonin. Biochim. Biophys. Res. Commun. 422, 97–102. PMID:22564742.
Techtmann SM, Lebedinsky AV, Colman AS, Sokolova TG, Woyke T, Goodwin L, Robb FT. (2012) Evidence for horizontal gene transfer of anaerobic carbon monoxide dehydrogenases. Front Microbiol. 3:132-145.
Lauro, F M, D. McDougald, T Thomas, T J Williams, S Egan, S Rice, M Z. DeMaere, L. Ting, Haluk Ertan, J Johnson, S. Ferriera, A. Lapidus, I. Anderson, N. Kyrpides, A. C Munk, C Detter, CS. Han, MV. Brown, FT. Robb, S Kjelleberg, and R. Cavicchioli. (2009) Feature Article: The genomic basis of trophic strategy in marine bacteria. Proc. Natl. Acad. Sci USA 106:15527-15533. Cover. PMID:19805210 | PMCID:PMC2739866
Luo H, Laksanalamai P, Robb FT. (2009) An exceptionally stable Group II chaperonin from the hyperthermophile Pyrococcus furiosus. Arch Biochem Biophys. 486:12-18. PMID:19298788
Sparks WB, J.H.Hough, L.Kolokolova, T.Germer, F.Chen, S.DasSarma, P.DasSarma, F.T. Robb, N.Manset, I.N.Reid, F.D.Macchetto, W.Martin (2009) Circular polarization in scattered light as a possible biomarker. JQSRT. doi:10.1016/j.jqsrt.2009.02.028
Techtmann, ST, AS Colman and FT Robb (2009) That which does not kill us only makes us stronger: The role of carbon monoxide in thermophilic consortia. Environ. Microbiol. 11(5):1027-37. PMID:19239487
Sparks WB, J.H.Hough, L.Kolokolova, T.Germer, F.Chen, S.DasSarma, P.DasSarma, F.T. Robb, N.Manset, I.N.Reid, F.D.Macchetto, W.Martin (2009) Detection of circular polarization in light scattered from photosynthetic microbes. Proc. Natl. Acad. Sci. USA. 106(19):7816-21
Wu, D, J. Raymond, M. Wu, S. Chatterji, Q. Ren, JE Graham, D.A Bryant, AS Colman, FT Robb, LJ Talon, J Badger, R. Madupu, NL Ward and JA Eisen (2009) Complete genome sequence of the CO-oxidizing extreme thermophile, Thermomicrobium roseum. PLoS One, 4(1):e4207.
Robb's main research interest is in hyperthermophiles that can survive and even thrive at temperatures up to 100°C (212°F), which in mere seconds can destroy DNA, "normal" proteins, and, hence, life. Dr. Frank Robb's main interest is learning specifically how these organisms can maintain stable proteins in the face of a thermal onslaught. His key focus is on heat shock proteins, known as chaperones, that the organisms produce to allow them to fold the proteins necessary for life. Robb and his colleagues are working toward various applications including using chaperones to improve high-temperature industrial or biomedical processes. The team, supported by the Bill and Melinda Gates Foundation, is exploring methods that seek to enhance the durability and immunogenicity of live vaccines through expression of heat shock proteins from thermophiles. If successful, the project will enable enhanced long term storage of vaccines in locations lacking refrigeration, for example in developing nations.
Another area of research is in tapping the thermophiles' penchant for producing hydrogen as a byproduct in order to develop new hydrogen production methods to add to the arsenal of technology needed for future supplies of renewable energy. Recent work has also focused on extremely stable cellulases for exploiting woody feedstocks for biofuel production.
The search for thermophiles has taken Robb to some exotic locales, including deep-sea hydrothermal vents, geothermal springs in the volcanic regions of New Zealand, Iceland, Eastern Russia's Kamchatka, as well as Yellowstone and Lassen National Parks.
Fellow, American Academy of Microbiology (2010-present).
Editor: "Thermophiles: Molecular Biology and Technology" (2009) and the "Extremophile Handbook" (2010),
Editor in Chief of Archaea: A Laboratory Manual (Cold Spring Harbor) (1995),
Editor, with Z Kelman and T Lowe: eBook on Frontiers in Genomic and Evolutionary Microbiology: Topic: Recent Advances in the Genetics and Genomics of Archaea (2013).
Scientific Advisory Board member, Genome Prairie, Calgary, Canada (2012-2015).
Faculty Member, Microbiology. Faculty of 1000 Prime. (2007-present).
Project Title:Compatible Solutes from Extremophiles for Cryopreservation of Live cells and Biomolecules
Institute of Marine and Environmental Technology (IMET) Post-Doctoral Research Program in Environmental and Marine Science, National Institute of Standards and Technology. $276,252
Award Period: 01/01/16 - 12/31/17.
Project Title:Sentinel Microbes that Utilize Carbon Monoxide as Energy and Carbon Source
National Aeronautics and Space Administration. $547,659
Award Period: 06/03/15 - 06/02/18
What is the hottest temperature life can survive?
BBC Earth (Quote)
January 10, 2016
Read story (www.bbc.co.uk)
Most organisms could not survive in the hot springs, says Frank Robb at the University of Maryland in Baltimore. “Temperatures at or near boiling basically cook normal biological material and destroy proteins, lipids and genetic material.” But high temperatures are not the only problem faced by organisms in the springs. Some pools are very acidic, close to pH2, whilst others are very alkaline and go up to pH10.5.
Some Like it Hot
Chemistry & Industry
June 7, 2016
Read story (www.soci.org)
Frank Robb, a researcher at the University of Maryland’s School of Medicine in Baltimore, US, has spent many years investigating how thermophiles maintain stable proteins in the face of intense heat. He has identified 'chaperone' or heat shock proteins that the thermophilic bacteria produce to allow them to fold the proteins necessary for life. These chaperone proteins continue functioning at high temperatures by refolding proteins that have denatured, stopping them from aggregating and sticking together.
Chaperones work on disordered proteins by binding specifically to them, and not to native proteins, and maintaining the solubility of their client proteins by obscuring their hydrophobic surfaces. Some classes of chaperones, like HSP60 or HSP70, are powered by ATP hydrolysis to actively fold proteins,’ explains Robb.
As well as molecular chaperones, Robb explains that thermophilic enzymes are also more compact and densely packed together than other enzymes, which minimises internal cavities in the hydrophobic core of the protein. Having smaller cavities, he says, makes the protein less susceptible to thermal denaturation because the core ‘resists conformational writhing and wriggling’.
Thermophilic enzymes also contain more ionic pair interactions between the amino acids. ‘Having extra ion pairs helps to make proteins more stable because the ion pair is effective over a much longer distance (over 3Ä) than van der Waals forces,’ says Robb. They also contain more acidic and basic amino acids and have more charged ions on their internal surface. As long as the charges are organised so that they exert attractive rather than repulsive forces on each other, this helps to hold the protein together.
IMET BOG Committee, 2010-2016
Chair, International Conference on Extremophiles, Cambridge, MD 2004. Program committee, Extremophiles 2006, 2008, Thermophiles 2007, 2009, Co-Chair: Workshop on Biogeochemistry and Molecular Biology of Thermophiles, Kamchatka August, 2000, 2005, 2010. Program Committee, Thermophiles 2007, 2017. Extremophiles 2010,2012,2016. Who's Who, 2013.
You wouldn’t last long if you jumped into a pool of boiling water. But some organisms on earth can thrive in such extreme environments and temperatures. They’re called thermophiles. Working at the Institute of Marine and Environmental Technology, Dr. Frank Robb of the University of Maryland School of Medicine is studying thermophiles to determine how they might benefit human health.